A peptide zipcode sufficient for anterograde transport within amyloid precursor protein.

A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Research Abstract Details 

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A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Abstract Text:

Prasanna Satpute-Krishnan,Joseph A DeGiorgis,Michael P Conley,Marcus Jang,Elaine L Bearer,

Fast anterograde transport of membrane-bound organelles delivers molecules synthesized in the neuronal cell body outward to distant synapses. Identification of the molecular "zipcodes" on organelles that mediate attachment and activation of microtubule-based motors for this directed transport is a major area of inquiry. Here we identify a short peptide sequence (15 aa) from the cytoplasmic C terminus of amyloid precursor protein (APP-C) sufficient to mediate the anterograde transport of peptide-conjugated beads in the squid giant axon. APP-C beads travel at fast axonal transport rates (0.53 mum/s average velocity, 0.9 mum/s maximal velocity) whereas beads coupled to other peptides coinjected into the same axon remain stationary at the injection site. This transport appears physiologic, because it mimics behavior of endogenous squid organelles and of beads conjugated to C99, a polypeptide containing the full-length cytoplasmic domain of amyloid precursor protein (APP). Beads conjugated to APP lacking the APP-C domain are not transported. Coinjection of APP-C peptide reduces C99 bead motility by 75% and abolishes APP-C bead motility, suggesting that the soluble peptide competes with protein-conjugated beads for axoplasmic motor(s). The APP-C domain is conserved (13/15 aa) from squid to human, and peptides from either squid or human APP behave similarly. Thus, we have identified a conserved peptide zipcode sufficient to direct anterograde transport of exogenous cargo and suggest that one of APP's roles may be to recruit and activate axonal machinery for endogenous cargo transport.

A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Publishing Authors By Initials

P Satpute-Krishnan,JA DeGiorgis,MP Conley,M Jang,EL Bearer,

For similar peptides: peptide fragments research abstracts see: peptides: peptide fragments research

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A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 103

Page Numbers: 16532-7

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 24

MONTH: 10

YEAR: 2006

A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Keywords Mesh Terms:

KEYWORDS: Peptide Fragments

MESH TERMS: metabolism

Chemical & Substance for Abstract: A peptide zipcode sufficient for anterograde transport within amyloid precursor protein. Information

Substance Name: Peptide Fragments

Registry Number: 0

Grant and Affiliation Information for A peptide zipcode sufficient for anterograde transport within amyloid precursor protein.

AFFILIATION: Department of Pathology and Laboratory Medicine, Brown University Medical School, 70 Ship Street, Providence, RI 02912, USA.

Country: United States

AGENCY: United States NINDS

GRANT: NS 046810

ACRONYM: NS

MEDLINETA: Proc Natl Acad Sci U S A

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